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Search results 101 to 150 out of 150 for Crb2

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Type Details Score
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database
Publication      
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
Publication
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
Publication        
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication      
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
Publication        
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
HT Experiment
Series Id: GSE50845
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: ArrayExpress
Publication
First Author: Quinn PM
Year: 2019
Journal: Hum Mol Genet
Title: Loss of CRB2 in Müller glial cells modifies a CRB1-associated retinitis pigmentosa phenotype into a Leber congenital amaurosis phenotype.
Volume: 28
Issue: 1
Pages: 105-123
Publication
First Author: Botuyan MV
Year: 2006
Journal: Cell
Title: Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair.
Volume: 127
Issue: 7
Pages: 1361-73
Publication
First Author: Sanders SL
Year: 2004
Journal: Cell
Title: Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage.
Volume: 119
Issue: 5
Pages: 603-14
DO Term
DO Term
Publication
First Author: Lu R
Year: 2013
Journal: Trends Biochem Sci
Title: Tudor: a versatile family of histone methylation 'readers'.
Volume: 38
Issue: 11
Pages: 546-55
Protein Domain
Type: Domain
Description: This is the tudor domain found in DNA repair protein Crb2. Structural and functional studies of Crb2 and its mammalian homologue 53BP1 indicate that the conserved tandem-Tudor domain of 53BP1 and Crb2 preferentially interacts with H4K20me2, though it also binds to H4K20me1 []. Furthermore, despite low amino acid sequence similarity, Crb2 is structurally related to 53BP1 in having two tudor domains and a conserved dimethyllysine-binding pocket, and that, like 53BP1, it directly binds H4-K20me2 [].
Protein Domain
Type: Family
Description: This entry represents fungal histone-lysine N-methyltransferase Set9 that belongs to the Suv4-20 family. This enzyme catalyzes mono-, di-, and trimethylation of H4K20. It participates in DNA damage response by giving a 'histone mark' required for the recruitment of the checkpoint protein Crb2 to sites of DNA damage [, ].
Publication
First Author: Wang Y
Year: 2009
Journal: Mol Cell
Title: Regulation of Set9-mediated H4K20 methylation by a PWWP domain protein.
Volume: 33
Issue: 4
Pages: 428-37
Protein Domain
Type: Domain
Description: This is one of two Tudor-like domains found in the N-terminal region of RapA proteins. RapA is an abundant RNAP-associated protein of 110kDa molecular weight with ATPase activity.It forms a stable complex with the RNAP core enzyme, but not with the holoenzyme. The ATPase activity of RapA increases upon its binding to RNAP []. The N-terminal region of RapA contains two copies of a Tudor-like domains, both folded as a highly bent antiparallel β-sheet. This fold is also found in transcription factor NusG , ribosomal protein L24, human SMN (survival of motor neuron) protein, mammalian DNA repair factor 53BP1, putative fission yeast DNA repair factor Crb2 and bacterial transcription-repair coupling factor known as Mfd. The functional roles of the N-terminal region homologs in these proteins suggest that the Tudor-like domains of RapA may interact with both nucleic acids and RNAP [].
Protein Domain
Type: Domain
Description: This is the second of two Tudor-like domains found in the N-terminal region of RapA proteins. RapA is an abundant RNAP-associated protein of 110kDa molecular weight with ATPase activity. It forms a stable complex with the RNAP core enzyme, but not with the holoenzyme. The ATPase activity of RapA increases upon its binding to RNAP []. The N-terminal region of RapA contains two copies of a Tudor-like domains, both folded as a highly bent antiparallel β-sheet. This fold is also found in transcription factor NusG , ribosomal protein L24, human SMN (survival of motor neuron) protein, mammalian DNA repair factor 53BP1, putative fission yeast DNA repair factor Crb2 and bacterial transcription-repair coupling factor known as Mfd. The functional roles of the N-terminal region homologs in these proteins suggest that the Tudor-like domains of RapA may interact with both nucleic acids and RNAP [].
Publication
First Author: Shaw G
Year: 2008
Journal: Structure
Title: Structure of RapA, a Swi2/Snf2 protein that recycles RNA polymerase during transcription.
Volume: 16
Issue: 9
Pages: 1417-27
Publication
First Author: Liu B
Year: 2015
Journal: Proc Natl Acad Sci U S A
Title: Structural basis for transcription reactivation by RapA.
Volume: 112
Issue: 7
Pages: 2006-10
Publication  
First Author: Richard M
Year: 2006
Journal: Hum Mol Genet
Title: Towards understanding CRUMBS function in retinal dystrophies.
Volume: 15 Spec No 2
Pages: R235-43
Protein Domain
Type: Family
Description: This entry includes Suv4-20 family members and its fungal homologue known as Set9. They are a group of histone H4K20 methyltransferases.SET9 methylates 'Lys-20' of histone H4. H4 'Lys-20' methylation is apparently not involved in the regulation of gene expression or heterochromatin function, but participates in DNA damage response by giving a 'histone mark' required for the recruitment of the checkpoint protein Crb2 to sites of DNA damage [, ].Post-translational modification of the core histones H2A, H2B, H3 and H4 play an important part in chromatin biology. Histone H4 lysine 20 methylation (H4K20me) is critical for the biological processes that ensure genome integrity, such as DNA damage repair, DNA replication and chromatin compaction []. Suv4-20 family members are a group of histone H4K20 methyltransferases that play an important role in epigenetic regulation. Lower eukaryotes have a single Suv4-20, while mammals have two closely related Suv4-20 paralogs, SUV420H1 and SUV420H2 []. In mammals H4K20me2 is generated primarily by SUV420H1/KMT5B (which can also produce H4K20me3), while H4K20me3 is mostly generated by SUV420H2/KMT5C [].
Protein
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 93  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 85  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 87  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1010  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1023  
Fragment?: false
Publication
First Author: Southall SM
Year: 2014
Journal: Nucleic Acids Res
Title: A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases.
Volume: 42
Issue: 1
Pages: 661-71
Publication
First Author: Tsang LW
Year: 2010
Journal: PLoS One
Title: Comparative analyses of SUV420H1 isoforms and SUV420H2 reveal differences in their cellular localization and effects on myogenic differentiation.
Volume: 5
Issue: 12
Pages: e14447
Publication
First Author: Jørgensen S
Year: 2013
Journal: Nucleic Acids Res
Title: Histone H4 lysine 20 methylation: key player in epigenetic regulation of genomic integrity.
Volume: 41
Issue: 5
Pages: 2797-806
Protein
Organism: Mus musculus/domesticus
Length: 883  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 468  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 423  
Fragment?: false